Chromatographic Purification of Highly Active Yeast Ribosomes

Chromatographic purification of highly active yeast ribosomes.

Eukaryotic ribosomes are much more labile as compared to their eubacterial and archael counterparts, thus posing a significant challenge to researchers. Particularly troublesome is the fact that lysis of cells releases a large number of proteases and nucleases which can degrade ribosomes. Thus, it is important to separate ribosomes from these enzymes as quickly as possible. Unfortunately, co...

Preparation of Highly Active Yeast Invertase*

In some preliminary experiments it was found that certain yeast invertase preparations which had been variously purified by adsorption to kaolin and alumina in accordance with the Willstiitter procedures (1) were soluble in saturated aqueous solutions of ammoniym sulfate. This solubility of the enzyme is interesting for two reasons. In the first place, saturated aqueous solution of ammonium sul...

Active yeast ribosome preparation using monolithic anion exchange chromatography

In vitro studies of translation provide critical mechanistic details, yet purification of large amounts of highly active eukaryotic ribosomes remains a challenge for biochemists and structural biologists. Here, we present an optimized method for preparation of highly active yeast ribosomes that could easily be adapted for purification of ribosomes from other species. The use of a nitrogen mill ...

Magnesium binding to yeast ribosomes.

Easy and Rapid Purification of Highly Active Nisin

Nisin is an antimicrobial peptide produced and secreted by several L. lactis strains and is specifically active against Gram-positive bacteria. In previous studies, nisin was purified via cation exchange chromatography at low pH employing a single-step elution using 1 M NaCl. Here, we describe an optimized purification protocol using a five-step NaCl elution to remove contaminants. The obtained...